GLYCO-N · GLYCOprotein N-glycosylation from non-life to eukaryotes: a Doctoral Network to expand the knowledge on a ubiquitous posttranslational modification of proteins
Horizon Europe — Marie Skłodowska-Curie Actions
- Duration
- 2024-02-01 → 2028-03-31
- EU contribution
- €2,677,118
- Participants
- 17
- Scheme
- HORIZON-TMA-MSCA-DN
Lines connect the coordinator with its partners.
Results in brief
GLYCOprotein N-glycosylation from non-life to eukaryotes: a Doctoral Network to expand the knowledge on a ubiquitous posttranslational modification of proteins
The GLYCO-N training network aims at training Doctoral Candidates (DCs) to acquire the skills to develop different innovative strategies to 1) understand the diversity and structural complexity of archaeal, microalgal and viral N-glycosylation and 2) harness this knowledge for new solutions in biomedicine and biotechnology. Protein N-glycosylation, or the attachment of oligo- and polysaccharides at specific asparagine residues, is conserved throughout life, and is now observed even in the viral world. In contrast to eukaryotes, whose well-studied N-glycosylation machineries are relatively simple, archaea, microalgae and bacteria utilize a wide variety of monosaccharides to create a wealth of structurally diverse N-glycans, and the same holds true for some recently discovered viruses. Because protein glycosylation occurs far downstream of protein synthesis the complexity and diversity in N-glycan structures are poorly understood in detail. This holds true specifically for Nglycosylation events that are the subject of the GLYCO-N program: those in archaea, microalgae and viruses. Understanding of the how and why of N-glycosylation in archaea, microalgae and viruses will open up many possibilities ranging from drug discovery (antivirals) to biotechnology (glycoprotein and glycoprocessing enzyme engineering for materials and life sciences). The GLYCO-N network brings together a diverse group of glycobiology researchers with world-leading expertise in microbiology, (bio)organic chemistry, computational and structural biology, bioinformatics and chemical biology. The GLYCO-N DCs will have their own individual project with one GLYCO-N expert and will, through research internships, be exposed to complementary Glycoscience. All individual PhD projects, while rooted in fundamental science, have a practical application, either in biotechnology or in biomedicine, as will be explored through secondments with our associated partners.
Data: CORDIS, © European Union
Project objective
The GLYCO-N training network aims at training Doctoral Candidates (DCs) to acquire the skills to develop different innovative strategies to 1) understand the diversity and structural complexity of archaeal, microalgal and viral N-glycosylation and 2) harness this knowledge for new solutions in biomedicine and biotechnology.Protein N-glycosylation, or the attachment of oligo- and polysaccharides at specific asparagine residues, is conserved throughout life, and is now observed even in the viral world. In contrast to eukaryotes, whose well-studied N-glycosylation machineries are relatively simple, archaea, microalgae and bacteria utilize a wide variety of monosaccharides to create a wealth of structurally diverse N-glycans, and the same holds true for some recently discovered viruses. Because protein glycosylation occurs far downstream of protein synthesis the complexity and diversity in N-glycan structures are poorly understood in detail. This holds true specifically for N-glycosylation events that are the subject of the GLYCO-N program: those in archaea, microalgae and viruses. Understanding of the how and why of N-glycosylation in archaea, microalgae and viruses will open up many possibilities ranging from drug discovery (antivirals) to biotechnology (glycoprotein and glycoprocessing enzyme engineering for materials and life sciences). The GLYCO-N network brings together a diverse group of glycobiology researchers with world-leading expertise in microbiology, (bio)organic chemistry, computational and structural biology, bioinformatics and chemical biology. The GLYCO-N DCs will have their own individual project with one GLYCO-N expert and will, through research internships, be exposed to complementary Glycoscience. All individual PhD projects, while rooted in fundamental science, have a practical application, either in biotechnology or in biomedicine, as will be explored through secondments with our associated partners.
Original text from CORDIS.
Participants
- UNIVERSITA DEGLI STUDI DI NAPOLI FEDERICO II · NapoliCoordinatorItaly
- ADAPTAM THERAPEUTICS SL · SAN SEBASTIANSpain
- ASOCIACION CENTRO DE INVESTIGACION COOPERATIVA EN BIOCIENCIAS · DERIO VIZCAYASpain
- ATLAS MOLECULAR PHARMA SL · DerioSpain
- Alga Biologics · IsneauvilleFrance
- DANMARKS TEKNISKE UNIVERSITET · Kongens LyngbyDenmark
- IMPERIAL COLLEGE OF SCIENCE TECHNOLOGY AND MEDICINE · LondonUnited Kingdom
- INNOVATION ACTA SRL · SIENAItaly
- Isuschem s.r.l. · NapoliItaly
- SAMABRIVA · AmiensFrance
- TECHNISCHE UNIVERSITAET DRESDEN · DresdenGermany
- THE FRANCIS CRICK INSTITUTE LIMITED · LondonUnited Kingdom
- UNIVERSIDAD DEL PAIS VASCO/ EUSKAL HERRIKO UNIBERTSITATEA · LeioaSpain
- UNIVERSITAET DUISBURG-ESSEN · EssenGermany
- UNIVERSITAT DE BARCELONA · BarcelonaSpain
- UNIVERSITE DE ROUEN NORMANDIE · MONT SAINT AIGNAN CEDEXFrance
- UNIVERSITEIT LEIDEN · LeidenNetherlands
Links
- View on CORDIS
- DOI: 10.3030/101119499
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e50aa4875b&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e51743bf66&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e522a3aa7e&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e522a3b196&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e528752f5c&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e528757782&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5287582ac&appId=PPGMS
Data: CORDIS, © European Union
